LicB

• Description: trigger enzyme: lichenan-specific phosphotransferase system, EIIB component
  
  

Gene name	licB
Synonyms	celA
Essential	no
Product	trigger enzyme: lichenan-specific phosphotransferase system, EIIB component
Function	lichenan uptake and phosphorylation, control of LicR activity
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	10 kDa, 6.314
Gene length, protein length	306 bp, 102 aa
Immediate neighbours	licC, licR
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU38590

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate (according to Swiss-Prot)

• Protein family: PTS permease, lactose permease (Lac) family PubMed

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on Ser-37 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions: LicB-LicC, LicB-LicR

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• Swiss prot entry: P46318

• KEGG entry: [2]

• E.C. number: 2.7.1.69 9

Expression and regulation

• Operon: licB-licC-licA-licH PubMed

• Sigma factor: SigA PubMed

• Regulation: repressed by glucose (CcpA) , carbon catabolite repression, induction by oligomeric ß-glucosides PubMed

• Regulatory mechanism: CcpA: transcription repression, catabolite repression: repression by CcpA, induction: transcription activation by the PRD-type regulator LicR PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040] [WorldCat.org] [DOI] (P p)

S Tobisch, P Glaser, S Krüger, M Hecker
Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis.
J Bacteriol: 1997, 179(2);496-506
[PubMed:8990303] [WorldCat.org] [DOI] (P p)

1. Reizer et al. (1999) Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis. Microbiology 145: 3419-3429 PubMed

1. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
2. Tobisch, S., P. Glaser, S. Krüger, and M. Hecker. 1997. Identification and characterization of a new ß-glucoside utilization system in Bacillus subtilis. J. Bacteriol. 179:496-506. PubMed
3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed